NMDA receptor trafficking through an interaction between PDZ proteins and the exocyst complex
Open accessAbstract
NMDA (N-methyl-D-aspartate) receptors (NMDARs) are targeted to dendrites and anchored at the post-synaptic density (PSD) through interactions with PDZ proteins. However, little is known about how these receptors are sorted from the endoplasmic reticulum and Golgi apparatus to the synapse. Here, we find that synapse-associated protein 102 (SAP102) interacts with the PDZ-binding domain of Sec8, a member of the exocyst complex. Our results show that interactions between SAP102 and Sec8 are involved in the delivery of NMDARs to the cell surface in heterologous cells and neurons. Furthermore, they suggest that an exocyst-SAP102-NMDAR complex is an important component of NMDAR trafficking.
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Exocyst-mediated AMPA receptor targeting, insertion, and recycling are thought to be independent of Ral.
“exocystmediated AMPA receptor targeting, insertion, and recycling (Sans et al, 2003;Gerges et al, 2006;Mao et al, 2010) are thought to be independent of Ral.”
From Ral mediates activity‐dependent growth of postsynaptic membranes via recruitment of the exocyst (2013) · cites this paper as Sans et al, 2003
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Montcouquiol, M., Sans, N., Huss, D., Kach, J., Dickman, J. D., Forge, A., Rachel, R. A., Copeland, N. G., Jenkins, N. A., Bogani, D., et al. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.4680-05.2006 · Cited by 322 · see citing works
Self-citationDurand, C. M., Perroy, J., Loll, F., Perrais, D., Fagni, L., Bourgeron, T., Montcouquiol, M., & Sans, N. (2012) · Molecular Psychiatry · doi:10.1038/mp.2011.57 · Cited by 316 · see citing works
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Self-citation
- Authors
- Sans, N., Prybylowski, K., Petralia, R. S., Chang, K., Wang, Y.-X., Racca, C., Vicini, S., & Wenthold, R. J.
- Affiliations
- National Institutes of Health (US)
- Georgetown University Medical Center (US)
- Corresponding author
- Sans, Nathalie
- Venue
- Nature Cell Biology
- Published
- 2003-05-12
- Volume
- 5
- Issue
- 6
- Pages
- 520-530
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- OpenAlex
- W2097424141
- Cited by
- 327
- References
- 2
- Citations by year
- 2026: 2 · 2025: 5 · 2024: 6 · 2023: 9 · 2022: 6 · 2021: 16 · 2020: 8 · 2019: 5 · 2018: 8 · 2017: 12 · 2016: 10 · 2015: 7 · 2014: 14 · 2013: 15 · 2012: 14
- FWCI
- 10.02
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Newcastle University ePrints (Newcastle Univesity)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Extracellular vesicles in disease
- Keywords
- NMDA receptor, receptor trafficking, PDZ domain proteins, exocyst complex, Sec8, SAP102, postsynaptic density, cell surface delivery, Golgi apparatus, endoplasmic reticulum, dendrite targeting
- MeSH terms
- Amino Acid Sequence, Animals, Brain Chemistry, Carrier Proteins, Cells, Cultured, Chlorocebus aethiops, Exocytosis, Membrane Proteins, Models, Biological, Molecular Sequence Data, Mutation, Neurons, Neuropeptides, Protein Binding, Receptors, N-Methyl-D-Aspartate, COS Cells, Protein Transport, Rats
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